Chlorine in PDB 232l: T4 Lysozyme Mutant M120K

All present enzymatic activity of T4 Lysozyme Mutant M120K:
3.2.1.17;

The structure of T4 Lysozyme Mutant M120K, PDB code: 232l was solved by L.A.Lipscomb, D.L.Drew, N.Gassner, W.A.Baase, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.73
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	60.930, 60.930, 96.680, 90.00, 90.00, 120.00
R / Rfree (%)	17.3 / n/a

The binding sites of Chlorine atom in the T4 Lysozyme Mutant M120K (pdb code 232l). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the T4 Lysozyme Mutant M120K, PDB code: 232l:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the T4 Lysozyme Mutant M120K


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of T4 Lysozyme Mutant M120K within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl173 b:6.2 occ:1.00 O A:HOH291 2.8 20.4 1.0 O A:HOH209 2.8 33.4 1.0 N A:ARG145 2.9 10.6 1.0 N A:ASN144 3.3 7.9 1.0 C A:THR142 3.4 13.4 1.0 CB A:THR142 3.4 14.2 1.0 O A:THR142 3.4 14.7 1.0 CB A:ARG145 3.4 10.3 1.0 CA A:THR142 3.5 8.5 1.0 O A:HOH214 3.7 33.4 1.0 CA A:ARG145 3.7 10.5 1.0 CA A:ASN144 3.8 8.6 1.0 C A:ASN144 3.8 14.6 1.0 CB A:ASN144 3.8 10.5 1.0 N A:PRO143 4.0 11.2 1.0 CG2 A:THR142 4.2 13.0 1.0 C A:PRO143 4.2 11.8 1.0 CD A:PRO143 4.4 12.3 1.0 O A:HOH230 4.5 32.6 1.0 OG1 A:THR142 4.5 13.6 1.0 CA A:PRO143 4.7 11.3 1.0 O A:HOH500 4.7 30.6 1.0 N A:ALA146 4.8 11.0 1.0 CG A:ASN144 4.8 38.5 1.0 C A:ARG145 4.8 13.1 1.0 O A:HOH237 4.9 27.2 1.0 CG A:ARG145 4.9 14.2 1.0 O A:ASN144 5.0 12.4 1.0 N A:THR142 5.0 9.5 1.0

Chlorine binding site 2 out of 2 in the T4 Lysozyme Mutant M120K


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of T4 Lysozyme Mutant M120K within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl178 b:10.5 occ:0.50 O A:HOH215 2.7 19.2 1.0 O A:HOH200 3.2 32.1 1.0 O A:HOH182 3.4 24.5 1.0 CB A:ALA49 3.9 14.7 1.0 CE1 A:HIS31 4.3 15.0 1.0 NE2 A:GLN69 4.3 17.3 1.0 NE2 A:HIS31 4.4 14.8 1.0 CA A:ALA49 4.5 14.2 1.0 CD2 A:LEU66 4.6 14.1 1.0 O A:ALA49 4.8 15.8 1.0

L.A.Lipscomb, N.C.Gassner, S.D.Snow, A.M.Eldridge, W.A.Baase, D.L.Drew, B.W.Matthews. Context-Dependent Protein Stabilization By Methionine-to-Leucine Substitution Shown in T4 Lysozyme. Protein Sci. V. 7 765 1998.
ISSN: ISSN 0961-8368
PubMed: 9541409